Antibodies, which are also known as immunoglobulins, are proteins that are produced by B-cells and that are used by organisms' immune systems to identify and neutralize foreign objects, such as bacteria, viruses, and other antigens. Generally, antibodies include a Y-shaped protein having two large heavy chains and two small light chains. Additionally, while the general structure of antibodies is generally similar, a small region at the tip of such proteins can be extremely variable, allowing for millions of antibodies with slightly different tip structures, or antigen binding sites. The region of a Y-shaped antibody protein that includes the antigen binding site is sometimes called the FAB (or the fragment, antigen binding) region. This FAB region, in turn, includes a constant domain (which remains constant across multiple types of antibodies) and one or more variable or hypervariable regions (which vary from one antibody to another) from each heavy and light chain of the antibody. The variable domains from the heavy chain (“VH”) and light chain (“VL”), which are part of the antibody's variable-region (or V-region), may be the most important parts of an antibody, and are responsible for binding the antibody to specific antigens.
While antibodies are well known for playing an important role in organisms' natural immune responses, antibodies have proven useful for a wide variety of other purposes. Indeed, antibodies have been found to be useful in many forms of medical diagnosis (e.g., in pregnancy tests, lupus diagnostic tests, etc.), in many research applications (e.g., to identify and locate intracellular and extracellular proteins), and even to treat a wide variety of diseases (e.g., rheumatoid arthritis, multiple sclerosis, psoriasis, cancer, etc.).
In the quest to find antibodies that can be used as therapeutic treatments for disease, there is a need to identify specific antibodies that are capable of effectively identifying and/or neutralizing antigens associated with a wide variety of diseases and maladies. Additionally, as many conventional methods for identifying such antibodies can be relatively inefficient and ineffective at identifying effective antibodies, it would be an improvement in the art to augment or even replace current techniques with other techniques.